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<p>Atomic crystal structure of activated [Fe]-hydrogenase</p>

In nature, hydrogenase enzymes mediate production and consumption of hydrogen (H2). However, hydrogenases are very sensitive to oxygen (O2) and heat, which restricts their applicability. Now scientists in Seigo Shima`s group have successfully solved the crystal structure of [Fe]-hydrogenase in its activated form, thus providing chemists with indispensable information for designing new robust and powerful H2 catalysts. more

<p>[Mn]-hydrogenase: A new step towards redesigning hydrogenases</p>

Hydrogen gas (H2) is proposed as a clean energy carrier for the future world - as long as its production works without the use of fossil fuels. Accordingly, there is intensive research on hydrogenases, enzymes that catalyze H2 production and consumption. Now scientists from MPI’s Shima group in cooperation with scientists from Lausanne were able to construct an active semisynthetic [Mn]-hydrogenase, thus providing a new way for designing and building new robust and efficient H2-activtion catalysts that might take part in future technologies. more

Hesse's Science Minister Angela Dorn visits the Max Planck Institute for Terrestrial Microbiology

On May 29, Angela Dorn, Hessian Minister of State for Science and the Arts, and Dr. Ulrike Mattig, Head of Department for Non-University Research Institutions, visited the Max Planck Institute for Terrestrial Microbiology at the Lahnberge in Marburg. more

It`s all about the Pole Position

Everyone following Formula 1 knows that securing the pole position is not simple. The same is true for many proteins in rod-shaped bacteria like Myxococcus xanthus: they must localize to the cell poles to function properly and getting to the pole is not a simple task. In a recent publication in Nature Microbiology, scientists from the Max Planck Institute for Terrestrial Microbiology together with scientists from the Technical University in Munich unraveled a novel mechanism for how a protein can get a pole position. more

<p>Discovery of [Fe]-hydrogenase in bacteria opens new possibilities for conversion of hydrogen</p>

Hydrogen gas is a green energy carrier. Microorganisms use dedicated enzymes, called hydrogenases to convert this gas into energy. One of the model enzymes is [Fe]-hydrogenase (Hmd) that catalyzes the reversible hydride transfer between H2 and the methanogenic C1-carrier tetrahydromethanopterin using a unique prosthetic group, the FeGP cofactor. Up to now, Hmd, its paralogue (HmdII), and the FeGP cofactor were identified only in archaea. Scientists at the Max Planck Institute for Terrestrial Microbiology in Marburg and collaborators at the Max Plank Institute for Biophysics in Frankfurt and Freie Universität Berlin now discovered that bacteria are also able to produce HmdII and the FeGP cofactor, and showed that bacterial HmdII uses the bacterial C1-carrier, tetrahydrofolate. This finding has a great potential for biotechnological development of Hmd variants that function in bacteria. more

A new way out!

A new way out!

April 01, 2019

Protein secretion is used by all cells to deliver proteins to different cellular compartments. In bacteria, proteins secreted to the extracellular milieu play key roles in a multitude of important processes including virulence, biofilm formation, adhesion, interactions between bacteria in microbiomes, host-microbe interactions, adaptation and motility. In a recent publication in Nature Communications, scientists from The Max Planck Institute for Terrestrial Microbiology together with scientists from the University of Montpellier describe a novel system for protein secretion by bacteria.  more

2019 Heinz Maier-Leibnitz Prize goes to Knut Drescher

Scientist at the Max Planck Institute for Terrestrial Microbiology receives Germany's most significant award for young scientists, the Heinz Maier-Leibnitz Prize, which is jointly awarded by the Deutsche Forschungsgemeinschaft (DFG) and the Bundesministerium für Bildung und Forschung (BMBF). more

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